Literature summary for 1.2.1.84 extracted from

Honsho, M.; Asaoku, S.; Fukumoto, K.; Fujiki, Y.
Topogenesis and homeostasis of fatty acyl-CoA reductase 1 (2013), J. Biol. Chem., 288, 34588-34598 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene far, recombinant expression of EGFP-tagged or FLAG-tagged wild-type and diverse truncation mutants of FAR in CHO-K1 cells, construction and expresion of several chimeric FAR1-FAR2 constructs in CHO-K1 cells, overview. Recombinant expression of N- and C-terminally HA-tagged Far1 in CHO-K1 and ZPEG251 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Experiments in which regions of Far1 or Far2 are replaced with the corresponding region of the other protein show that the region flanking the transmembrane domain of Far1 is required for plasmalogen-dependent modulation of Far1 stability. Expression of Far1 increased plasmalogen synthesis in wild-type Chinese hamster ovary (CHO) cells. FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview. Mutants FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. Expression of FLAG-tagged mutant Far1490-Far2 increases plasmalogen synthesis	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview	Homo sapiens	-	-
peroxisomal membrane	Far1 is a tail-anchored type II peroxisomal membrane protein. The transmembrane segment of Far1 is located in its C-terminus region (amino acids 466-483). The hydrophobic C-terminus of Far1 binds to Pex19p, a cytosolic receptor harboring a C-terminal CAAX motif, which is responsible for the targeting of Far1 to peroxisomes. The C-terminus of Far1 is exposed to the peroxisome matrix, whereas a large catalytic domain in its N-terminus is located outside of peroxisomes	Homo sapiens	5778	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
a long-chain acyl-CoA + 2 NADPH + 2 H+	Homo sapiens	-	a long-chain alcohol + 2 NADP+ + coenzyme A	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q8WVX9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
a long-chain acyl-CoA + 2 NADPH + 2 H+	-	Homo sapiens	a long-chain alcohol + 2 NADP+ + coenzyme A	-	?

Synonyms

Synonyms	Comment	Organism
FAR1	-	Homo sapiens
fatty acyl-CoA reductase 1	-	Homo sapiens
peroxisomal fatty acyl-CoA reductase 1	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	the NADPH-binding domain corresponds to amino acids 15-285	Homo sapiens

General Information

General Information	Comment	Organism
additional information	FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. FLAG-Far1 is largely resistant to trypsin digestion and is partially digested upon incubation with a large amount of trypsin	Homo sapiens
physiological function	peroxisomal fatty acyl-CoA reductase 1 (Far1) is essential for supplying fatty alcohols required for ether bond formation in ether glycerophospholipid synthesis. The stability of Far1 is regulated by a mechanism that is dependent on cellular plasmalogen levels. Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Far1 is a rate-limiting enzyme for plasmalogen synthesis. The transmembrane-flanking region of Far1 is required for its plasmalogen-dependent degradation	Homo sapiens

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Release 2023.1 (January 2023)